Ph.D. in Biotechnology, Department of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden, 2009
Group leader at the Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany
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Carlon, A., Ravera, E., Hennig, J., Parigi, G., Sattler, M. and Luchinat, C. (2016). Improved Accuracy from Joint X-ray and NMR Refinement of a Protein-RNA Complex Structure. J Am Chem Soc 138(5): 1601-1610.
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Horn, A., Hennig, J., Ahmed, Y. L., Stier, G., Wild, K., Sattler, M. and Sinning, I. (2015). Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction. Nat Commun 6: 8875.
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Loedige, I., Jakob, L., Treiber, T., Ray, D., Stotz, M., Treiber, N., Hennig, J., Cook, K. B., Morris, Q., Hughes, T. R., Engelmann, J. C., Krahn, M. P. and Meister, G. (2015). The Crystal Structure of the NHL Domain in Complex with RNA Reveals the Molecular Basis of Drosophila Brain-Tumor-Mediated Gene Regulation. Cell Rep 13(6): 1206-1220.
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Freiburger, L., Sonntag, M., Hennig, J., Li, J., Zou, P. and Sattler, M. (2015). Efficient segmental isotope labeling of multi-domain proteins using Sortase A. J Biomol NMR 63(1): 1-8.
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Hennig, J., Warner, L. R., Simon, B., Geerlof, A., Mackereth, C. D. and Sattler, M. (2015). Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements. Methods Enzymol 558: 333-362.
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Hennig, J. and Sattler, M. (2015). Deciphering the protein-RNA recognition code: combining large-scale quantitative methods with structural biology. Bioessays 37(8): 899-908.
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Friberg, A., Thumann, S., Hennig, J., Zou, P., Nossner, E., Ling, P. D., Sattler, M. and Kempkes, B. (2015). The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation. PLoS Pathog 11(5): e1004910.
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Hennig, J., Andresen, C., Museth, A. K., Lundstrom, P., Tibell, L. A. and Jonsson, B. H. (2015). Local destabilization of the metal-binding region in human copper-zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS. Biochemistry 54(2): 323-333.
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Hennig, J., Gebauer, F. and Sattler, M. (2014). Breaking the protein-RNA recognition code. Cell Cycle 13(23): 3619-3620.
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Hennig, J., Militti, C., Popowicz, G. M., Wang, I., Sonntag, M., Geerlof, A., Gabel, F., Gebauer, F. and Sattler, M. (2014). Structural basis for the assembly of the Sxl-Unr translation regulatory complex. Nature 515(7526): 287-290.
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Feige, M. J., Grawert, M. A., Marcinowski, M., Hennig, J., Behnke, J., Auslander, D., Herold, E. M., Peschek, J., Castro, C. D., Flajnik, M., Hendershot, L. M., Sattler, M., Groll, M. and Buchner, J. (2014). The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins. Proc Natl Acad Sci U S A 111(22): 8155-8160.
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Loedige, I., Stotz, M., Qamar, S., Kramer, K., Hennig, J., Schubert, T., Loffler, P., Langst, G., Merkl, R., Urlaub, H. and Meister, G. (2014). The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation. Genes Dev 28(7): 749-764.
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Hennig, J. and Sattler, M. (2014). The dynamic duo: combining NMR and small angle scattering in structural biology. Protein Sci 23(6): 669-682.
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Wang, I., Hennig, J., Jagtap, P. K., Sonntag, M., Valcarcel, J. and Sattler, M. (2014). Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1. Nucleic Acids Res 42(9): 5949-5966.
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Pfaff, J., Hennig, J., Herzog, F., Aebersold, R., Sattler, M., Niessing, D. and Meister, G. (2013). Structural features of Argonaute-GW182 protein interactions. Proc Natl Acad Sci U S A 110(40): E3770-3779.
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Weininger, U., Blissing, A. T., Hennig, J., Ahlner, A., Liu, Z., Vogel, H. J., Akke, M. and Lundstrom, P. (2013). Protein conformational exchange measured by 1H R1rho relaxation dispersion of methyl groups. J Biomol NMR 57(1): 47-55.
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Weininger, U., Blissing, A. T., Hennig, J., Ahlner, A., Liu, Z., Vogel, H. J., Akke, M. and Lundstrom, P. (2013). Protein conformational exchange measured by 1H R1rho relaxation dispersion of methyl groups. J Biomol NMR 57(1): 47-55.
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Hennig, J., de Vries, S. J., Hennig, K. D., Randles, L., Walters, K. J., Sunnerhagen, M. and Bonvin, A. M. (2012). MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry. BMC Struct Biol 12: 29.
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Wennerstrand, P., Dametto, P., Hennig, J., Klingstedt, T., Skoglund, K., Appell, M. L. and Martensson, L. G. (2012). Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: a biophysical characterization of TPMT*2 and TPMT*5. Biochemistry 51(30): 5912-5920.
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Espinosa, A., Hennig, J., Ambrosi, A., Anandapadmanaban, M., Abelius, M. S., Sheng, Y., Nyberg, F., Arrowsmith, C. H., Sunnerhagen, M. and Wahren-Herlenius, M. (2011). Anti-Ro52 autoantibodies from patients with Sjogren's syndrome inhibit the Ro52 E3 ligase activity by blocking the E3/E2 interface. J Biol Chem 286(42): 36478-36491.
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Hennig, J., Hennig, K. D. and Sunnerhagen, M. (2008). MTMDAT: Automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins. Bioinformatics 24(10): 1310-1312.
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Hennig, J., Bresell, A., Sandberg, M., Hennig, K. D., Wahren-Herlenius, M., Persson, B. and Sunnerhagen, M. (2008). The fellowship of the RING: the RING-B-box linker region interacts with the RING in TRIM21/Ro52, contains a native autoantigenic epitope in Sjogren syndrome, and is an integral and conserved region in TRIM proteins. J Mol Biol 377(2): 431-449.
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Ottosson, L., Hennig, J., Espinosa, A., Brauner, S., Wahren-Herlenius, M. and Sunnerhagen, M. (2006). Structural, functional and immunologic characterization of folded subdomains in the Ro52 protein targeted in Sjogren's syndrome. Mol Immunol 43(6): 588-598.
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Hennig, J., Ottosson, L., Andresen, C., Horvath, L., Kuchroo, V. K., Broo, K., Wahren-Herlenius, M. and Sunnerhagen, M. (2005). Structural organization and Zn2+-dependent subdomain interactions involving autoantigenic epitopes in the Ring-B-box-coiled-coil (RBCC) region of Ro52. J Biol Chem 280(39): 33250-33261.
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Ottosson, L., Salomonsson, S., Hennig, J., Sonesson, S. E., Dorner, T., Raats, J., Kuchroo, V. K., Sunnerhagen, M. and Wahren-Herlenius, M. (2005). Structurally derived mutations define congenital heart block-related epitopes within the 200-239 amino acid stretch of the Ro52 protein. Scand J Immunol 61(2): 109-118.